Role of Ser216 in the Mechanism of Action of Membrane-bound Lytic Transglycosylase B: Further Evidence for Substrate-assisted Catalysis
Lytic transglycosylases cleave the β-(1 → 4)-glycosidic bond in the bacterial cell wall heteropolymer peptidoglycan between the N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues with the concomitant formation of a 1,6-anhydromuramoyl residue. Based on sequence alignments, Ser216 in Pseudomonas aeruginosa membrane-bound lytic transglycosylase B (MltB) was targeted for replacement with alanine to delineate its role in the enzyme’s mechanism of action.
Recommended CitationReid, Christopher W.; Legaree, Blaine A.; and Clarke, Anthony J., "Role of Ser216 in the Mechanism of Action of Membrane-bound Lytic Transglycosylase B: Further Evidence for Substrate-assisted Catalysis" (2007). Science and Technology Faculty Journal Articles. Paper 41.